ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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Q6MS67 | MFSNWDIFLNYKNFTINQEIKNKLDLYYQILIQENQKYNLTRITELNEVFEKHFLDSLLFVEQFQIIDQKIADIGTGAGFPGIVLKIFFPNIKLTLIESNNKKANFLKYLVQKLELNNVEILNKRAEELNEYKEHLI | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 16349
Sequence Length: 137
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
P75220 | MNNSKLKQYVQLVQTANQNFNLTGLKTEGEIYEHLVQEIIELFNEYDSYFDHKKVADLGSGNGCPGVILKLLFPQIKTLDLIDSKHKKVNFLKEVIQTLELNNTQALCARIENHTEQYDTLCSRGLGSIIEVNAFALKLLKPNGIIFHIKQSLDQYLEFEDSEQKDQFKPLFFKFFHGKRQQILIAMKKNV | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 22080
Sequence Length: 191
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q98R82 | MNCLEKITNEYGQKTASRLEQFVKLIEEENKKINLTSFEGQRLWQEGIYESIKCLEPFVKSNDSLLDIGAGVGFPSVPFLIVNPEVKLTIIESNKKRVLFLEKVKKDLNLSFEIFNGRVENFNKEIHFDFITARALAPLNILMELTINLGSILPKPTNYIFVKGANYLSELNEAQNAIKILKLKVFDLKKIDVFFDKNIFMIHYIKTANVSKEYPRAWDKIIKKPIR | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 26276
Sequence Length: 227
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
A0R7J5 | MKHGSVPATPEAASLVFGDRLEAAELYARILAGAGVEWGLLGPREVDRVWERHILNSAALGELMEPGERVADIGSGAGLPGIPLALARPDIHVTLIEPLLRRSEFLRETVTELGLDVTVVRGRAEDREVRDRVGEMDVVTSRAVASLDKLTRWSVPFLRDGGRMLPIKGERAEVEIEEHRRVMESLGAVDARVVRCGANYLSPPVTVVDARRRAAKPGRNKSGRTARSRGRTGRR | Function: Specifically methylates the N7 position of guanine in position 518 of 16S rRNA.
Sequence Mass (Da): 25732
Sequence Length: 235
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q4A6Q0 | MEFKNKVIAYCKERNANFLDFEKYVSLIEEHNKNINLTGFSGESLWEEGILNSLLYMNSSTKDKSEIKILDIGSGVGFPAIPYALLRENNSIDIFEPIQKRVDFLNLVKQKLTLDKVNIYKQRAEEFSQKNIYDVVVARAVGSVKTMLMAAFHLVALKGEMVLIKGPKYKQEILEAQEILSKLKVEVIVDKFILNAKENFLVRIKKLRNCPKEFPYSWKDIKKQS | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 25986
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q30TL7 | MNLKTALLELDTELPDTFFHHIQKFKEHLFKWNKIHNLTGAKDENTIDEFIYDAIYPITFLPKCKNLLDIGTGAGFPGLILAMGLPETEVTLVEPLAKRASFLQFIKADLGLSNVKVVQKRVQDMPSEIFEIVTSRAVIDTNMLLELSKGFRNKDSKLLFFKGERVYDEVNKDLKYKIIKRENRHYLLIGETL | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22245
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
A6QC07 | MQYLNAEGIVLDDGIIGKLEGFAVLLHEWNQVHNLTGARSVVAIYDNIVDSLYPLTFIRIPKTLLDVGTGAGFPGLVLAIALPETEVVLAEPLKKRVSFLKYAAIDLGLKNVTVEAKRVENVVYEAFDMISSRAVTNTKLLLDLTSRISDEHTEYLFYKGSRVFDEIAQVEGQMSYDIIQKNQRNYLYIKNET | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 21672
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
Q67J35 | MDATAYRGLLEEGLASLGVEAEPGGVEAVLLHLDLVREWNERMNLTAITDPQEMVIKHALDAASGLAVAGVEPGQRVIDVGTGAGFPGVVWKCLRPGIDLTLLESLQKRCRFLEEVGQAVIGPLAGGEGYQVVWGRAEDVGRNPAHRERYDLVTARAVAELRVLAEYCLPLARVGGRFLAMKGPSVGEEILAAEAAVEKLGGRLEEVRELELPDGGGRRSLVLIRKERPTPKAYPRRAGVPAKSPL | Function: Specifically methylates the N7 position of a guanine in 16S rRNA.
Sequence Mass (Da): 26424
Sequence Length: 246
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q2LY85 | MIRLLNNFNFSEIDNADPAQWCRLFQEAAAEFDVLLSDAQLNRFLMYYRELKFWNSRINLIASAESVTDIVIKHFLDSLTLIPCIPFPDGRLIDIGTGGGFPGIPLKIALNSLKVTLLEASRKKVSFLKSLRRVLNLQDMKILNERVEDLITQAPCPNRFDMVVSRAALKLPEYLRFGKELVSSHGVIIAMKGANYQHELEDVNDILEEYGIFLAEVRSLALPCTGDFRAILIFRKSLSRT | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27379
Sequence Length: 241
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
Q39ZT2 | MQNRLQELLTRIGLSLEKPVCDRLLWYLDEMLRWNRRINLTAIENKEEALEKHLLDSLTVVPLLRGDERLLDMGSGAGLPSIPIKIARPQMCVLSVDSVHKKIVFQQHVARQLKLQGFEARACRIQSLSQGESETSFDVVTARALTHLSDLLSMAEPLLNDKGRLIAMKGPDGEAELAECAQQIRKAGFVAEPLQHLSLPLSGSERTLVVLKRKPGR | Function: Specifically methylates the N7 position of guanine in position 527 of 16S rRNA.
Catalytic Activity: guanosine(527) in 16S rRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(527) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24302
Sequence Length: 217
Subcellular Location: Cytoplasm
EC: 2.1.1.170
|
Q7VQJ5 | MFIMHHNSVLLHEAINALNINPSGIYIDGTFGLGGHSHYILSKLTSHGRLIAMDRDWSAVNIGEVLTKQDGRFSIIHAPFSKMLRCIYNMNLVGLINGILLDLGVCESQLTDSSRGFSFMRDGPLDMRMDNSVGQSAYEWIAKASQKDIEWVLRTFGEEKLSKKIARSIVLKREVYPIDRTSALSEIISDTVLYYNNRYNRRKHPATRSFLAIRIYINEELVEIMKILQDVFKLLAPGGRLVVISFNSLEDRIVKKFINQYSRVFAYPPKIPLTHTQLLHKYSGTMKFKNLGKIKPTVLEIKKNIRARSAILRYAEKLIYM | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36798
Sequence Length: 321
Subcellular Location: Cytoplasm
EC: 2.1.1.199
|
Q2KVE4 | MKFEHRPVLLEPTVDALLQADFGGRGASRARPRDEAAALTRQATGIFVDGTFGRGGHSRELLGRLGPQARLVVFDKDPEAIAVAQALAAEDARVTVVHGGFATMTEELAARGIERIDGVMLDLGVSSPQIDDADRGFSFMREGPLDMRMDTSRGPTVADWLAQASVEEMREVIADYGEERFAFQVAKAIAARRATRPLHTTLELAECVASAVRTREKGQHPATRTFQALRIYINRELEELARALASAIELLVPGGRLAVISFHSLEDRMVKQCIAAAARPAAAHPRLPLRESELPQPILQTLGKVVADDAEVAGNARSRSAILRAAERTSQPLPATGAEDFVPAVPGAAEKGRRR | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 38344
Sequence Length: 355
Subcellular Location: Cytoplasm
EC: 2.1.1.199
|
O51286 | MNNNAFHFPVLLDAICKLIEDLPVKSDLIYIDSTLGEGVHAKAILEKYDFLSLVGIERDPQILERARQFLSIFEERITYFNDWFDNFFVNYPLNVKANFILVDLGISMFHYKGSKKGFSFLEDEPLDMRLCSSSCKISAAEIVNTYSKYDLEALIYDLSNEHYSRRISKAIVEYRKIKKIETTKELQSIISKVYPFSKVKINPATKTFQALRIYVNDELARLKRSLPFWVENLAKDGILAIITFHSIEDRIVKDFFRSLSCDLYAKISKKPIMPSFDEIKKNKPSRSAKLRVVKKL | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34382
Sequence Length: 296
Subcellular Location: Cytoplasm
EC: 2.1.1.199
|
Q89FT9 | MSSAPHIPVLGREAIDHLAPREGGIYVDATFGAGGYSRAILDVPGTRLIAIDRDRTAIAGGAELVERSAGRLTLVEDRFSHLADVCAAQGVDAVDGVVMDVGVSSMQLDQAGRGFSFRLDGPLDMRMGQAGPTAADVVARASEADLADIIYLLGEERHSRRVARAIVADRQETPFTTTRALADLVGRVVRSKPGDIHPATRTFQALRIFVNEELEELQTALTAAERVLKPGGRLVVVSFHSLEDRIVKNFLAERSKTGGGSRHLPEVAQTAPSFQLLTRRPVVAGEDEVAHNPRARSAKLRAAERTSAPAHKDDQSSSWPRLSDVMRGG | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35347
Sequence Length: 329
Subcellular Location: Cytoplasm
EC: 2.1.1.199
|
C5B9E8 | MSENFQHKTVLLDEAVAGLNLRSDGIYIDGTFGRGGHSRLILSQLGAEGRLIAIDRDPQAIAAAAQIDDPRFSIIHGPFSALADYVQEMGLSSRIDGILLDLGVSSPQLDDPERGFSFMRDGPLDMRMDPSRGLSAAQWLMQAEEDDIAWVLKTFGEERFAKRIARAIVERNRTEPLSRTRELAALISDASPFKEKHKHPATRSFQAIRIYINSELDEIERALEGALVALAPQGRLSVISFHSLEDRLVKRFIRQYSRGPQVPKGLPLTEAQLQAQGGPQLKALGKRMPGEREVVDNPRARSSVLRVAERIAR | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34753
Sequence Length: 313
Subcellular Location: Cytoplasm
EC: 2.1.1.199
|
Q8YRT9 | MTKTPLTIEEPIFSHLPVLPQEVITGLVVRPGGRYLDVTVGGGGHSRLILEAAPDVKLTAVDQDGDALTAAKQELAEFGEQVKFVRSNFAAYDFPSTSFDGVLADLGVSSYHLDTPERGFSFRHQASLDMRMDQRQSLSAADVINDWDEVELANIFFKYGEERLSRRIARRIVEKRPFHTTTELAEAIASSVPPKYRYGRIHPATRVFQALRIVVNDELKSLETFIEKAPKALVPGGRIAIISFHSLEDRLVKHGLRNSPLLKVLTKKPIIATDDEIANNPRSRSAKLRIAEKQAETGDEDN | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33612
Sequence Length: 302
Subcellular Location: Cytoplasm
EC: 2.1.1.199
|
Q2G9A3 | MSAETGSRAPHIPVLLEEVVAALDPKPGDLIVDATFGAGGYTRRLLDAGATVHAFDRDPDAIAAGKLWGETCGKEPRLVLHPRRFSEIAEGLAEAGIAGVQGVVFDIGVSSMQLDQAARGFAFSSDGPLDMRMSQEGPSAADFLNEADEGEIADVLYRYGEERQSRRIARAIVAARPLTTTAQFAAVVRKALGYRPDIKGPKAPKDPATRSFQAVRIHVNGELDELVQGLAAAEKVLVPGGRIAVVSFHSLEDRIVKQFLREGAGAVPAGSRHLPQLESKVQAVFEKPSGAIRPTPEEEARNPRARSATLRCAVRTAAPARAHQGRAAA | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34987
Sequence Length: 329
Subcellular Location: Cytoplasm
EC: 2.1.1.199
|
Q313R1 | MTADNGHDNNRHQYTAHVPVLLDEVLHYLSPVRGGRYLDGTLGLGGHSEAIMNRCGGDAWLLGLDRDREALAAASGRLAPFGDRVTTRYACYSQFAAIMDEIGWTGLDGALIDIGVSSMQIDTPSRGFSFYADGPLDMRMDPSGDMPSAGVLVNTGSVERLKEIISTYGEDPMAGRIARAIVDARARNPIETTARLAEVVESAYPAKWRAKSRNHPATRTFQALRMAVNGELEELETFLAAIVDRMNPGGRIVVITFHSLEDRLVKNAFRDEAKGCLCPRHIPVCVCGKKPRVNVLTRKPVTAGQAELQANSRASSAKLRAAERI | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35388
Sequence Length: 325
Subcellular Location: Cytoplasm
EC: 2.1.1.199
|
P60397 | MNKTHFNHISVLKQEAIDFLKIKPEGIYVDATLGQCGHTIEIANLLQQGFLYSFDQDVEACTNAKKILPPHLPIEIIHSNFSHLKTQLAQRNVFQLDGILFDLGLSSCQIDNPQRGFSYLHNTPLDMRMNVNQTITAQYILNNYSFAQLKNIFKVYGEVKNAALVASEIIKQRPLCTSYDLVAITDRFCNRQKGHSAKKIFQALRIEVNQELESLKQALEQSLDLLKPNAMIVVISFHSLEDRIVKHFFKKNSTFVLPKKMPITIMPQTPLSIITKKAFLPSEEEMQNNSRSISAKLRVAVKNG | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34555
Sequence Length: 304
Subcellular Location: Cytoplasm
EC: 2.1.1.199
|
B1ZU25 | MTPGHQPVLLREVLGFLAPRARGRYLDCTFGGGGHTRALLEAAAEVRVVALDRDPAAQPRAAALRETFGERFEFIDRDFGRLAELPHEGFDGVLFDFGVSSFQLDETERGFSFRHDAPADMRMDPRSGVPASQWLETATEEMLVRAIRDFGEEQHWRRIVRAIRDARGTGALARTASLAELIAAAIPACDRHAAKIHPATRAFQGVRIAVNDEIGAIERALPAAFAKLAPGGVLCVISFHSLEDRPAKQFFRRMCGQPESAADATPQDLRVKLADPLTRRPVTPADDELAANPRSRSAKLRALRRL | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33675
Sequence Length: 306
Subcellular Location: Cytoplasm
EC: 2.1.1.199
|
A5CD85 | MNNIHTPVMATEMLSYLAPVDNETYLDCTFGTGGYSKLILSNCNCKIIAFDRDPAVISIASQFYQQYSNRFTFFNDNFVEANKYLSKSAKLNGIVMDLGVSSMQLDAANRGFSFRYDAELDMRMSQKGYKASELVNEASEHQLADIIYKFGEENKANKIAKHIVLAREKKPITTTLQLANIIREAVGYNNYYKKNKIDSATKTFQAIRIFINDELSAIQNFLNQSLELLAVNGRLIVVSFHALEDAIVKKFMHQNAVKKVAQSKYSTNKQLPLQNGVLHLLTKKIAVPTRTEIINNPRSRSARLRAALKINE | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35267
Sequence Length: 312
Subcellular Location: Cytoplasm
EC: 2.1.1.199
|
Q01Q40 | MHVPVMPAEAIELLAIRPEGVYLDATAGLGGHSGLIARQLTTGTVIANDRDTRSLEMARANTAEWSDRMCFHYGSFGSLSDAVSQAGFEKVDGLLADLGVSRYQLTAPDRGFSFMADGPLDMRMDASIQTTAADLVNHTDEKTLADLIYQMGEERRARRIARAIVRARPLRSTLHLADVVERAVPRTGRLHPATKTFMALRMAVNDEPGELRRLLEIAPGLLKSGGRMVVISFMSSDDRMVKEKFKELGQSKQATILTKHPLQPSDEESFNNPASRSAKLRALEMR | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 31505
Sequence Length: 286
Subcellular Location: Cytoplasm
EC: 2.1.1.199
|
A9FI25 | MNVVNVVPMHLPPPPPRPRGEQHVSVLGREVLAALSPVSEGVYVDATLGAGGHTATILETPGARVIGIDRDERALAIARARLARAGDRVTYVHGEFSEIERHLAALGVPQVDGLLADIGVSSMQLDDPGRGMSFRAEGPLDMRMDSSRGETALELIERLSDEELADLIYRYGEERRSRRVARCIKQAADSGELVTTLDLRRAVVRAVGPARIGGVDPATRTFQALRIAVNGELDQLEALLEAAPRIIAPGGVLAVISFHSLEDRIVKRALREPEVWEPLTKKPVTAGDDEVEGNPRARSAKLRAARRVGGAEALA | Function: Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Catalytic Activity: cytidine(1402) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(4)-methylcytidine(1402) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33913
Sequence Length: 315
Subcellular Location: Cytoplasm
EC: 2.1.1.199
|
Q0A6F5 | MINRNHRPLRGVLSDPDEPAAAAALAHRLDLPLLTEPPETPALFLHHSRNGLALRSSGSNAPGPIRVSLDEGRQGQRLRQASLKRETLARACGLRGGRSLRIVDATAGLGRDAMVLAALGARVTLIERHPVIAALLADGLRRARRSHPELAARLHLVEADSLQWLAELTPAERPEVICLDPMYPAGSTRGAVRKDLQALRELPDWPGLAPVDEVALLALARASATARVVVKRPGRAAPLAGKAPDWQLPGRSTRFDVYRGLAGD | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28378
Sequence Length: 264
Subcellular Location: Cytoplasm
EC: 2.1.1.242
|
B4S2X7 | MLNSVPLVIAQHSTQDDTSLLNSIGNKWGFPVVSHSEKPAEGFYLQIQNGVLGLADASEKKVLPVEVDFASPASLYRKQHGGGRKEPIVKAIGLKGNEGWHVVDATPGLGRDAFVLVSVGCKVTMIERSPIVAALLEDGIRRLALSFPELAAKMSLQHGNSAEVMQYFTGENVNAIYLDPMFPHKKKSALVKKEMRLFQQLLGHDPDADALLPPALKLATHRVVVKRPNSADVLAGEKPSMAIESKKHRFDVYLCQKP | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28163
Sequence Length: 258
Subcellular Location: Cytoplasm
EC: 2.1.1.242
|
Q6MQB7 | MVSASLDGGLRICVRASAPEVHDKAVAWASFLKAPLNPENPEQYFFHFFVEPEGVYVRDQEKRLLEIDFDKNHLDYERKGHRGKNELIAKALGVAKGARRILDLSVGMGIDSVFLTQLGFSVIGVERSPVLYALLKEAFARTKKDSLKSYELHFADSLQFLKQNKGLLEVDAIYFDPMYPHKKKSALPKQEMVVFRDLVGHDDDASLVLQEALTWPVKRVVVKRPMQAEELLPGVRHSYEGKVVRYDTYVVG | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28576
Sequence Length: 252
Subcellular Location: Cytoplasm
EC: 2.1.1.242
|
P57646 | MKIYLKFKSYNKRICKLLQLFKLEHDQNCSMGLLINHNSLELYNRDNVNQKPIKVDFTSKKNHYRCHHFRRKNEVLYRVSGIKNSYFPTILDATAGLGNDAFIFSFLGCKVIMIERHPIVAALLKDGLQRGYQDKKIGHWLQTRLHLIVNDSLKMLEIPILQPDVIYLDPMYPFHHKKSLPKKDMQFFRQLIGHNYDSKKLLEVSRKLAKNRIIVKRPYYAKPLSEDKVNHIVTTRNHRFDIYQPF | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29240
Sequence Length: 246
Subcellular Location: Cytoplasm
EC: 2.1.1.242
|
B3PLF9 | MLSIPLVCSSDFAPAAQVLAQEFNLPIRVGEVPETIGDCEFVLVLDETGLALQQTGRKAPGAVRAEFTEGAVDHRRKFGGGKGQMIAKAVGVKAGFSPRVLDATAGLGRDAFVLATLGCRLQMIERSPLVFALLRDGLARAHAFAHAQDRELLQVVERMELAAQDSKTYLQGLAPEQFPDVIYLDPMFPERQKSADVKKEMRAFHSIVGTDEDADVLLPLALEHVRFRVVVKRPRKAPFLNNQIPSYQLEGKSSRYDIYTRKKLPD | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29370
Sequence Length: 266
Subcellular Location: Cytoplasm
EC: 2.1.1.242
|
Q7P0V2 | MTATPLYCAEPARLDTARRLCERFSLPLIKQRPADGYWLELGSERLELLTTGKHGAVYAEFVEGAARHRREQGGGRGQPVAKAVGLKGAKDLPHVADATAGLGRDSFVLATLGCRVTMVERSPVAAALLADALERAQRDETTRDIAARMTLVHANSRNWLAGLTEAQRPDVVFVDPMFPDTDKKSAAAKKDMQAFQQVIGDDMDSAELLAAAIAAARVRVVVKRPRLGAAIAGVKPSAVLDGKSTRFDLYVIKALASG | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27673
Sequence Length: 258
Subcellular Location: Cytoplasm
EC: 2.1.1.242
|
A9KB94 | MNDTLAITYSTPARLSEAEKLARQMKLPLVSLNSTDYSFLLVFTPAHLELRSTGTKAPGPLYVDFLKGATAHRRLFGGGRSQLIVRAVGLKSHPHPTILDLTAGLGRDAFVLANFGCDVLMIERNPVIALLLRDGLERAQSVEWFKSLKLELIEIDAQIYLSTLKKQFDVIYMDPMYPIRKKSALVKKEMRILRRLVGADDDAPQLLALALKKAKHRVVIKRPLLSNPLPGPAPDVVYEGKSSRFDVYLLKPSS | Function: Specifically methylates the guanosine in position 1516 of 16S rRNA.
Catalytic Activity: guanosine(1516) in 16S rRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(1516) in 16S rRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28302
Sequence Length: 254
Subcellular Location: Cytoplasm
EC: 2.1.1.242
|
Q03516 | MNSTNSTNSTTTATSTNTSTQQVVTSLVSNGTIFGVFVIAFLILRIKLKRIYEPKSSFNLINEEKKPEPLPQGVWQWLKPLLKKSDNFVIQQAGLDGYFFLRYLFIIAIYCAVSMSYIFPILLSINASNGNHESGLNQLAYQNVKHRGRYFAHVFCGWIFFWGFLYIIYRELYFYTSMKQAVLASPRYAKKLSSRTVLFQTVPKQYLSEEEFSKLFDGVKRVWIARGSGSIEAMVKARDNMAIQLEGAETKYLKAALKKIKKLNKKSPQLSVSDNIAEYVPDKKRPHHKINKVAKFFFGKKVDTISYIKEELPKLNQKVKALQEDHENSSPFNSVFVEFESQYQAQVAAQITTYHAPLFMTPVYIGIEPSDVVWFNLRMFWWERLGREVSAVSAIVALVILWAFPVAFVGMISNITSLTNEVKWLKFIYKLPKQLLGLLTSLAPTVALAVLMSFLPKFIRGMAITQGAPSKQNVEYFTQQAYFAFQVIQVFLVTTLSSAATSTVTEIVKEPTKAMDLLASNLPKASNFFMSYVILQGLSISSGALLQIVPLILFYVLGAFLDGTVRKKWNRFCGLSSMQWGTAFPVYTNLAVITFSYSIISPLILLFAAVAFFLLYIAYLYNLTYVYQESPDARGIYYPRALFQTIVGIYIGQICLLGLFAVGKGWGPIVLQVIGICVTVLIHLHLSAAFDHLSKVIPVDTMKPLDGVSDTPSFKNIYKGIESTKVKKNTFGANIDMDGIKELPEFPIKKYHKRSESVTEQQVENSIFSENTFEYQFNPANEANADGHAINAENLIEDVPLLADGDTMKIPPAPWWKRFLKPHIYYSYKAVKSRLPEIYGLVDPDERVNDFDISHAYDYPAVSAQCPELWIPRDPFGFSKLLISDVSGVVEMNDENATIDENLKFTLRDVPPPYNDVKDEANGEANGEFDTASKENNPFADPKYKEEESRSAV | Function: Acts as an osmosensitive calcium-permeable cation channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 107673
Sequence Length: 953
Subcellular Location: Membrane
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Q23121 | MAARIYIGRLTSRVSEKDIEHFFRGYGQIRDVLLKNGFGFVEFDDKRDAEDAVHDLNGKELGGERVILDYSKPRGGGGDRGGFGGGGRGGARVSSYSGGGGGGRDRFDRYDRGPPRRESRYGRPYSTRHRVVVENLSSRISWQDLKDQVRRQGVEPTYAEAHKRPNEALLCFATPSDLKRCIEKCDGMDLNGRKIKMIDDSQAGRSRSRSNSRSRSRSRSRDRRRSRSRSSSRSKSRSRSPPKRSRRESKSKSRSRSRSRSADNRKSRSPSRSPKKVDRSPSPPRGSRSPSEKGSPRRSRSASPMDNGDGDN | Function: Plays a functionally redundant role in spermatogenesis and growth rate control.
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 35042
Sequence Length: 312
Subcellular Location: Nucleus
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Q27YU0 | MALGPFVLPFRGDQYSFGINFKSSPEEKLNFDLSCVAFDVKGQLHDTLHARKPTALDGALVKGFEKQALPEETVQVEGDDVIYMFPKKFERQVEVLLFVASAPSIPGKKHDLDSSSKLEFAVSYSDVGGQAFNQSFDLKPLAAQGGVSSIIVAVMYLQAEGGWTLRSVGDCHPFDSPGLIVPELKQTILNLRDHHGVQLDAADAIQAIDPAERVPVTRQFQDQSLDEASAGRAAEPAPVKKLRIDLSWTFWPPPPPTEEGEEPPEEPALEYNLVMYNKDGEEVQSISTGNREATGARAGRPEPEEDEEEEKEEEKEEPEEGEEGEEGEGGEPKEPPPPPPAPKVDPYEFKERDVIYLDVPDLPAEVRSMVLLVTNYDEENGFTRVRTVRCRLVDVSNGEAPLPGSKAAVAAAAAAAEQGLAAPPNPERVLADYGVLSKYEDDKATTQVALMKLYKEYADSAFNVFRGAGVDNVAAFIGQEPDTIINQLKAYLEATKKQKAAEAAAAAAAEESGEEITADPKPHVWRFRALGLNFGGDSLEAIEHDLKNLFAFDGDLAPGAARDSDTSRSSFPNGDTYFGSYADDVKHGPGLYAFATGAGYAGEYAGGKRHGRGVMVFPDGGTYVGEFVADKFEGQGQYRYPDGSVYTGSWAAGQKHGPGVYWDTARGCLRGEWKKGLLVGKGTYEQPALRFEGEFVRGMPAGTATYTLTGHRTLDMPCFAAQHIQAEEGPTLALPCAYGIPPGSGDEPQLDEEGQPIEDTDKPPLPAHPKYEGLTFTAEQLPGAAPDTVFPPEEGKPVPITAVPAFSVSTGLVA | Function: Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to the a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules.
PTM: Asymmetrically dimethylated at Arg-243 and Arg-428 during flagellum resorption. Probably methylated by PRMT1.
Sequence Mass (Da): 87786
Sequence Length: 814
Subcellular Location: Cytoplasm
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Q23120 | MVRVYIGRLPNRASDRDVEHFFRGYGKLSDVIMKNGFGFVDFQDQRDADDAVHDLNGKELCGERVILEFPRRKVGYNEERSGSGFRGREPTFRKGGERQFSNRYSRPCSTRFRLVIDNLSTRYSWQDIKDHIRKLGIEPTYSEAHKRNVNQAIVCFTSHDDLRDAMNKLQGEDLNGRKLKCTDETRDRSRSRSPRRRSRSRSPTRSRSPPARRRSPGSDRSDRKSRSASPKKRSDKRARSESKSRSRSGGRRSRSNSPPNRSPSPKKRRDNSSPRSGSASP | Function: Plays a functionally redundant role in spermatogenesis and growth rate control. Required for the development of somatic gonad structures and for progression from larval stage to adulthood.
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 32421
Sequence Length: 281
Subcellular Location: Nucleus
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Q6UBQ3 | MAPTQAGHDTAYLKETVGEALARGCAAAISAQPNDPVEYLGLWLLKYVKNAEVEGNFYRERQQDLQKKKDRLVKEAQSEQAAKSVALTRKEAADALALVTAEPRELLEAAVKLVKQHTAAGAAYAAVVAEPEEPDWVAPEDDEAAAVETEDEAAGGAALAEGEEPPPEPEPEPEAAPEDGEGDAPAPKIPRPVDYSKKYFAYVAASAGQEHVLEADLYRPAPPPEDADEDFKPEPLPYSFRVLDEKLPMLYVPNVAAEERVKFFRKFPKIGSYQACGVALPASGEFKALLAADTLFPEGSGQPLSADDRDFVWEVSQSLSRALEAVQARAAEALAATSAAEAVEELKAKVAELREQAAAEAAAAAPPPPAEGEEGEGEAPPAEEEPPAEEEAEEEEEEAEEGAEEGAEEGEEGEEAPPKPKKKKKVFNPIPGLQAAIEKLTAAAEAATEADARAQAAVALEKQALDEVVALASSHSDATLSSLRNMLSVPQGTYHVVKALLHLLGRPAASFSTWKRAHSHFSPRLFEDMAAYDATAERDMAVWGRVRSCYKAAPAAKKLDAEMPNTLFGSVALMYIKQVRRVARKAVLQRELAAKLAKAQQDLADKQAALVEAERVKAEREAEEARLAAEAEAAAAAEAEAAARAAAEAEAAAAAEAAAEAAAEAAAAAAEAAAEAGEGEAVAEREAAPAEAEAAPAEGEAAPPAEGEGEAQPAQEGSNSSSSSSDSSSSEESKAAAE | Function: Flagellar radial spokes contribute to the regulation of dynein arm activity and thus the pattern of flagellar bending. They consist of a thin stalk, which is attached to the a subfiber of the outer doublet microtubule, and a bulbous head, which is attached to the stalk and appears to interact with the projections from the central pair of microtubules . Binds calmodulin in a calcium-dependent manner .
PTM: Asymmetrically dimethylated at Arg-104, Arg-260, Arg-453, Arg-538 and Arg-615 during flagellum resorption. Probably methylated by PRMT1.
Sequence Mass (Da): 77363
Sequence Length: 738
Subcellular Location: Cytoplasm
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Q9NEW6 | MPRGGSEDQKVYVGNLPGDVREKEVEDIFHKYGRIKYVDIKSGRGPAFAFVEFEDHRDAEDAVRARDGYEFDGRRIRVEFTRGVGPRGPGGRPLQDGGDHRGGDFRGGRGGGRGGGPQRRTGYRVIVEGLPPTGSWQDLKDHMRDAGDVCYADVARDGTGVVEFTRYEDVKYAVRKLDDTKFRSHEGETAYIRVREDNSSGGGSGGGGRDRSRSRSPRAERRASPKYSPRRSRSRSRSRSRSRSRSASRSPSRSPSPQ | Function: Plays an essential role in embryogenesis.
PTM: Directly phosphorylated by spk-1 in vitro on serine residues of the RS domain.
Sequence Mass (Da): 28680
Sequence Length: 258
Subcellular Location: Nucleus
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P12759 | MVQAKAQQQLYTHAAEPKAVQQRRAKYREDETTQTLPTANIMFDRRVVRGNTYAARILPADATQTQTKGPSPASTKKRTTRTLPPRTPEAVDGRRHIDIQTDVYLEELTDTVPEADTSTQTDAFLDRPPTPLFVPQKTGTDAITQIENGDLFDFDFEVEPILEVLVGKVLEQGLMEVLEEEELAAMRAHQEHFEQIRNAELVATQRMEAAERRKLEEKERRMQQERERVERERVVRQKVAASAFARGYLSGIVNTVFDRLVSSGYIYDPVMREVETAFMPWLKEQAIGYLARGVVARRVVDKLVEDAAAALAANRSTLADKAASTAATVDAWAERQAKMEAELQGKELEAVRRRPTFVLRELKPAVASADAVEAAAAELTAQAEEAANAKWEADKAEAAEKARAEAEAAAEEQKALLEELAATAAAEAEERGEEPPAEPPSLPDGVEPVDVEAEVAKAVEAVPKPPVKEVTDIDILSYMMDKGAITKDAIIQALAVHALGDKAYTNHPAFAEAEGA | Function: Protein 3 may attach the radial spoke to the outer doublet microtubule or is required to form a stable spoke structure.
PTM: Protein 3 is one of the 5 radial spoke proteins that are phosphorylated.
Sequence Mass (Da): 56785
Sequence Length: 516
Subcellular Location: Cytoplasm
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Q09511 | MSRGGGGDRRAAPDINGLTSLKIDNLSYQTTPNDLRRTFERYGDIGDVHIPRDKYSRQSKGFGFVRFYERRDAEHALDRTDGKLVDGRELRVTLAKYDRPSDERGGRGGGGGRRRSRSPRRRSRSPRYSRSRSPRRSRSRTRSPPSRDRRDSPDRRDNSRSRSRSPPPREDGSPKERRSRSRSASRSPSRSRSNSR | Function: May play a functionally redundant role in embryogenesis.
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 22588
Sequence Length: 196
Subcellular Location: Nucleus
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P52108 | MNTIVFVEDDAEVGSLIAAYLAKHDMQVTVEPRGDQAEETILRENPDLVLLDIMLPGKDGMTICRDLRAKWSGPIVLLTSLDSDMNHILALEMGACDYILKTTPPAVLLARLRLHLRQNEQATLTKGLQETSLTPYKALHFGTLTIDPINRVVTLANTEISLSTADFELLWELATHAGQIMDRDALLKNLRGVSYDGLDRSVDVAISRLRKKLLDNAAEPYRIKTVRNKGYLFAPHAWE | Function: Member of the two-component regulatory system RstB/RstA.
PTM: Phosphorylated by RstB.
Sequence Mass (Da): 26704
Sequence Length: 239
Subcellular Location: Cytoplasm
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P18392 | MKKLFIQFYLLLFVCFLVMSLLVGLVYKFTAERAGKQSLDDLMNSSLYLMRSELREIPPHDWGKTLKEMDLNLSFDLRVEPLSKYHLDDISMHRLRGGEIVALDDQYTFLQRIPRSHYVLAVGPVPYLYYLHQMRLLDIALIAFIAISLAFPVFIWMRPHWQDMLKLEAAAQRFGDGHLNERIHFDEGSSFERLGVAFNQMADNINALIASKKQLIDGIAHELRTPLVRLRYRLEMSDNLSAAESQALNRDISQLEALIEELLTYARLDRPQNELHLSEPDLPLWLSTHLADIQAVTPDKTVRIKTLVQGHYAALDMRLMERVLDNLLNNALRYCHSTVETSLLLSGNRATLIVEDDGPGIAPENREHIFEPFVRLDPSRDRSTGGCGLGLAIVHSIALAMGGTVNCDTSELGGARFSFSWPLWHNIPQFTSA | Function: Member of the two-component regulatory system RstB/RstA. RstB functions as a membrane-associated protein kinase that phosphorylates RstA (Probable).
PTM: Autophosphorylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 49283
Sequence Length: 433
Subcellular Location: Cell inner membrane
EC: 2.7.13.3
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P0AA45 | MRLDKFIAQQLGVSRAIAGREIRGNRVTVDGEIVRNAAFKLLPEHDVAYDGNPLAQQHGPRYFMLNKPQGYVCSTDDPDHPTVLYFLDEPVAWKLHAAGRLDIDTTGLVLMTDDGQWSHRITSPRHHCEKTYLVTLESPVADDTAEQFAKGVQLHNEKDLTKPAVLEVITPTQVRLTISEGRYHQVKRMFAAVGNHVVELHRERIGGITLDADLAPGEYRPLTEEEIASVV | Function: Responsible for synthesis of pseudouridine from uracil-516 in 16S ribosomal RNA.
Catalytic Activity: uridine(516) in 16S rRNA = pseudouridine(516) in 16S rRNA
Sequence Mass (Da): 25865
Sequence Length: 231
EC: 5.4.99.19
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Q9CPN4 | MRLDKFLAENTGLTRSQANKVLKQSAVTVNGHVEKNGAQKVSQTDEICLEGEHLPWVSAGQYLMLYKPQGYVCSHEDGDYPTIYQFFDYPLAGKLHSAGRLDVDTTGLVLLTDDGKWSHRITSPKHHCEKTYLVTLADPVESHYQQACAEGMLLRGEKTPTKPATLEILDDYNVNLTISEGRYHQVKRMFAALGNKVVGLHRWKIGQIELDDRLAEGEYRSLSAEEIATFNK | Function: Responsible for synthesis of pseudouridine from uracil-516 in 16S ribosomal RNA.
Catalytic Activity: uridine(516) in 16S rRNA = pseudouridine(516) in 16S rRNA
Sequence Mass (Da): 26096
Sequence Length: 232
EC: 5.4.99.19
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P77285 | MLKTIRKHGITLALFAAGSTGLTAAINQMTKTTIAEQASLQQKALFDQVLPAERYNNALAQSCYLVTAPELGKGEHRVYIAKQDDKPVAAVLEATAPDGYSGAIQLLVGADFNGTVLGTRVTEHHETPGLGDKIELRLSDWITHFAGKKISGADDAHWAVKKDGGDFDQFTGATITPRAVVNAVKRAGLYAQTLPAQLSQLPACGE | Function: Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane (By similarity). Required to maintain the reduced state of SoxR. Probably transfers electron from NAD(P)H to SoxR .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21912
Sequence Length: 206
Subcellular Location: Cell inner membrane
EC: 7.-.-.-
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O81127 | MTRVYVGNLDPRVTERELEDEFKAFGVLRNVWVARRPPGYAFLEFDDERDALDAISALDRKNGWRVELSHKDKGGRGGGGGRRGGIEDSKCYECGELGHFARECRRGRGSVRRRSPSPRRRRSPDYGYARRSISPRGRRSPPRRRSVTPPRRGRSYSRSPPYRGSRRDSPRRRDSPYGRRSPYANGV | Function: Probably involved in intron recognition and spliceosome assembly.
PTM: Extensively phosphorylated on serine residues in the RS domain (By similarity). Phosphorylated by AFC2.
Sequence Mass (Da): 21537
Sequence Length: 187
Subcellular Location: Nucleus speckle
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Q6K4N0 | MARLYVGNLDPRVTSGELEDEFRVFGVLRSVWVARKPPGFAFIDFDDKRDAEDALRDLDGKNGWRVELSRNSSSRGGRDRHGGSEMKCYECGETGHFARECRLRIGPGGLGSGKRRSRSRSRSRSPQYRKSPTYGRRSYSPRDRSPRRRSVSPVRGRSYSRSPRGRGGSPYADGRDGGRYRRSRS | Function: Involved in pre-mRNA splicing.
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 21023
Sequence Length: 185
Subcellular Location: Nucleus
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O81126 | MSRVYVGNLDPRVTERELEDEFRAFGVVRSVWVARRPPGYAFLDFEDPRDARDAIRALDGKNGWRVEQSHNRGERGGGGRGGDRGGGGGGRGGRGGSDLKCYECGETGHFARECRNRGGTGRRRSKSRSRTPPRYRRSPSYGRRSYSPRARSPPPPRRRSPSPPPARGRSYSRSPPPYRAREEVPYANGNGLKERRRSRS | Function: Sequence-specific RNA-binding protein probably involved in pre-mRNA splicing. In vitro, can complement efficiently splicing-deficient mammalian SRSF7-depleted HeLa cell extract.
PTM: Extensively phosphorylated on serine residues in the RS domain. Phosphorylated by AFC2.
Sequence Mass (Da): 22458
Sequence Length: 200
Subcellular Location: Nucleus speckle
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Q9FYB7 | MPRYDDRYGNTRLYVGRLSSRTRTRDLERLFSRYGRVRDVDMKRDYAFVEFSDPRDADDARYYLDGRDFDGSRITVEASRGAPRGSRDNGSRGPPPGSGRCFNCGVDGHWARDCTAGDWKNKCYRCGERGHIERNCKNSPSPKKARQGGSYSRSPVKSRSPRRRRSPSRSRSYSRGRSYSRSRSPVRREKSVEDRSRSPKAMERSVSPKGRDQSLSPDRKVIDASPKRGSDYDGSPKENGNGRNSASPIVGGGESPVGLNGQDRSPIDDEAELSRPSPKGSESP | Function: Probably involved in intron recognition and spliceosome assembly.
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 31823
Sequence Length: 284
Subcellular Location: Nucleus
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Q8VYA5 | MPRYDDRYGNTRLYVGRLSSRTRTRDLERLFSRYGRVRDVDMKRDYAFVEFGDPRDADDARHYLDGRDFDGSRITVEFSRGAPRGSRDFDSRGPPPGAGRCFNCGVDGHWARDCTAGDWKNKCYRCGERGHIERNCKNSPKKLRRSGSYSRSPVRSRSPRRRRSPSRSLSRSRSYSRSRSPVRRRERSVEERSRSPKRMDDSLSPRARDRSPVLDDEGSPKIIDGSPPPSPKLQKEVGSDRDGGSPQDNGRNSVVSPVVGAGGDSSKEDRSPVDDDYEPNRTSPRGSESP | Function: Splicing factor involved in constitutive and/or alternative splicing. Regulates the splicing of its own pre-mRNA and the alternative splicing of RS30, RS31 and RS34. Associates the cyclin-dependent kinase G1 (CDKG1) with the spliceosome and recruits it to U1 snRNP to facilitate splicing.
PTM: Extensively phosphorylated on serine residues in the RS domain.
Sequence Mass (Da): 32893
Sequence Length: 290
Subcellular Location: Nucleus speckle
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P23070 | MKSAEYLNTFRLRNLGLPVMNNLHDMSKATRISVETLRLLIYTADFRYRIYTVEKKGPEKRMRTIYQPSRELKALQGWVLRNILDKLSSSPFSIGFEKHQSILNNATPHIGANFILNIDLEDFFPSLTANKVFGVFHSLGYNRLISSVLTKICCYKNLLPQGAPSSPKLANLICSKLDYRIQGYAGSRGLIYTRYADDLTLSAQSMKKVVKARDFLFSIIPSEGLVINSKKTCISGPRSQRKVTGLVISQEKVGIGREKYKEIRAKIHHIFCGKSSEIEHVRGWLSFILSVDSKSHRRLITYISKLEKKYGKNPLNKAKT | Function: Reverse transcriptase (RT) component of antiviral defense system retron Ec86, composed of a non-coding RNA (ncRNA), a ribosyltransferase/DNA-binding protein and this RT. Expression of the 3-gene retron confers protection against bacteriophage T5. At multiplicity of infection (MOI) of 0.02 cultures grow normally when infected with T5 without collapsing, at MOI 2 cultures enter growth stasis . Responsible for synthesis of msDNA (a branched molecule with RNA linked by a 2',5'-phosphodiester bond to ssDNA). The retron transcript serves as primer (from a conserved internal G residue) and template for the reaction, and codes for the RT . Recognizes only its cognate RNA as a primer template . Overexpression of the ncRNA and RT (without the ribosyltransferase), which leads to increased levels of msDNA, is mutagenic in vivo . This may be due to a mismatch in the msDNA stem which binds and sequesters MutS and/or MutL (Probable).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 36424
Sequence Length: 320
Domain: The C-terminal domain (residues 230-320) is required to recognize and bind RNA; recognition of cognate RNA also requires a region closer to the N-terminus.
EC: 2.7.7.49
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P0DV59 | MKTKKMILVDKVFYEKILSVESFKENIITQSAIPKISNKEVRLISSGSKIFYAINNTSPHSHVQLRLNRFFLSHIPLNSAAKAFVRGGSYLKYLEPHIYGSSYCRLDISSFFNNISFDDVKQSLSPYIKDEYLIGTEQKLIDAILNSVGYESPIRKDKGMIIPMGFRTSPAISNIVFRKMDLLIQDFCAKKGVIYSRYADDMLFSNPRESKLLMSDYFIDEISSLLSIMGFNINQSKYISREKEISINGYVIENKGGNGSIGTIRLSKSKLNTVLKVTHALAQNIPYKNICNKYIKVRLKEKNIKYESKKDEFEKKYYRDQLINYLGGYRSYLISLVKFHSEYKCVNSDFIIQINGILNDIQNHIQKIKKNRRL | Function: Reverse transcriptase (RT) component of antiviral defense system retron Eco8, composed of this RT, the following endonuclease and a non-coding RNA (ncRNA) encoded between them. Expression of retron Eco8 confers protection against bacteriophages T4, T6, T7 and SECphi4, SECphi6 and SECphi18. At multiplicity of infection (MOI) of 0.02 cultures slow growth when infected with SECphi4 but do not collapse, at MOI 2 cultures collapse. Responsible for synthesis of msDNA (a branched molecule with RNA linked by a 2',5'-phosphodiester bond to ssDNA). The retron transcript serves as primer (from a conserved internal G residue) and template for the reaction, and codes for the RT.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 43208
Sequence Length: 374
EC: 2.7.7.49
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P0DV94 | MNILTTLREQLLTNNVIMPQEFERLEVRGSHAYKVYSIPKRKAGRRTIAHPSSKLKICQRHLNAILNPLLKVHDSSYAYVKGRSIKDNALVHSHSAYVLKMDFQNFFNSITPTILRQCLIQNDILLSVNELEKLEQLIFWNPSKKRNGKLILSVGSPISPLISNAIMYPFDKIINDICTKHGINYTRYADDITFSTNIKNTLNKLPEIVEQLIIQTYAGRIIINKRKTVFSSKKHNRHVTGITLTNDSKISIGRSRKRYISSLVFKYINKNLDIDEINHMKGMLAFAYNIEPIYIHRLSHKYKVNIVEKILRGSN | Function: Reverse transcriptase (RT) component of antiviral defense system retron Vc95, composed of a non-coding RNA (ncRNA), this reverse transcriptase (RT), a probable ATPase and a putative HNH endonuclease. Expression of retron Vc95 confers protection against bacteriophages T2, T4 and T6. At multiplicity of infection (MOI) of 0.02 cultures slow growth when infected with T4 but do not collapse, at MOI 2 cultures enter growth stasis . Responsible for synthesis of msDNA (a branched molecule with RNA linked by a 2',5'-phosphodiester bond to ssDNA). The retron transcript serves as primer (from a conserved internal G residue) and template for the reaction, and codes for the RT (By similarity). The DNA segment is predicted to be 95 bases long (Probable).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 36388
Sequence Length: 315
EC: 2.7.7.49
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B2KWI0 | MSPESKKITAHGSTSMPLSRTSKPQKFTIPLTVGAIFSVIGFLQRFFLASGKGDVQSLYTLSTMFILGAGPTYAGADYFICGRLFSFVPSAAPMSPIRVVRTFITFDVLAEVCVWTGAGLLAGAHTDTAARYKIGLNLIRAAMITQAFLFTSFVAILASFHVRVCALRAEWSVTSNGGTGRRFMMVVHSLYASSIFIIIRSAYHIAGHSFRTNEQPFLICEASLMLLNTAMFNVFHPGHILPIDSRVYVGIDGQERANETIEGAFTDSRPLLQKILDPLDVKGLFSRDKKRWHDPTAELEMDINSTLYAALT | Function: Lipid-translocating exporter-like protein; part of the gene cluster that mediates the biosynthesis of hydroxamate-containing siderophores that play a critical role in virulence via intracellular iron acquisition during macrophage infection .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34277
Sequence Length: 312
Pathway: Siderophore biosynthesis.
Subcellular Location: Membrane
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E5AE43 | MNAYAYTACLGIYGSTPNNEQLVLGSPDQLQRNKPRFRLIVLPHAPAASPFYPPWRSFAPDWEGQGARPMDHFKVGNLRFQLETHRIDEHSTFGKLFGHAPSPSQSCVSFQKKSDRAEPLLLARCSAASWSCIHPPTVLYFVAYQLEYPFAARFSATKISPIQDKMVATSDVPIVGSLYVYAPNKGAPIFFTIAFAISTILHSWQCHRYKAWKLIWLQPACAALFTLGYALREYGAYNYLYDGTEKAPLALFILSQICIYLGPPLLELANYHILGRVFHYVPYAAPFNPGRVTAFFGGLMAIVEGLSGSGVSLTANAKAKESTKKTGHNLLLVALALQVCVIFIFVYLSVLFHRRCIKAKVPAQSKAVKSTLMTLYLSMALIFIRCVFRLVEMATSSTSVDITSMERLMKLSPVLRNEAYFYAFEASLMLINSFLWNVQHPGPHLPGDTHIYLAQDGTEVEGEGDGSEDRPLLLNMANTLMFGLLYRDDKDHTHSQPQELYENPNGNGHKKFRLGNGGRAT | Function: Lipid-translocating exporter-like protein; part of the gene cluster that mediates the biosynthesis of phomenoic acid, a long chain aliphatic carboxylic acid that does not appear to be essential for pathogenicity but may play a role in allowing to outcompete other fungi in the environmental niche via its antifungal properties.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58112
Sequence Length: 521
Subcellular Location: Membrane
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P53047 | MAKDGFELYRYTPELGASILFTVLFAVSGVAFVILLFHYSVKSKRRVGSLMKSQPVLRYYGTVNLAGAYIPFIFGCFVECVGFAFRCKSSKDTTLLNPYIIQTVFLLVSPTLYAASIYMIFGRMATLLFAENLMIMPARFNTTIFVIGDVGSLLLQAIGGAMMSKVTSASSGSHLVTAGLFIQIAFFGLFIINEVLFIFKMSKKPTNVSVRYGSWKYLNIALLVNSFLILIRSIVRAVEFIQGYDGEIASHEWYLYIFDGLPMFLLVLIFIVAFPLINIFRIHEESIQAQQSARFDGTDYPDVEVTSIEEDLASKSE | Function: Involved in 7-aminocholesterol resistance.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35486
Sequence Length: 317
Subcellular Location: Membrane
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Q9BSG5 | MDCRVHMRPIGLTWVLQLTLAWILLEACGGSRPLQARSQQHHGLAADLGKGKLHLAGPCCPSEMDTTETSGPGNHPERCGVPSPECESFLEHLQRALRSRFRLRLLGVRQAQPLCEELCQAWFANCEDDITCGPTWLPLSEKRGCEPSCLTYGQTFADGTDLCRSALGHALPVAAPGARHCFNISISAVPRPRPGRRGREAPSRRSRSPRTSILDAAGSGSGSGSGSGP | Function: Riboflavin-binding protein which might have a role in retinal flavin transport.
PTM: Not N-glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 24615
Sequence Length: 229
Subcellular Location: Secreted
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Q5DRQ5 | MACRSHIQPSDLACTMQLALAWIILGACGGSHQFQARSQGHLGLASNLGTNQVQLAGDLQASGPQPYMMIQDPDSQAFPLPEPCCPSEMDTPETSGPGIFPPRCRTPSSGCESFLGHLQRALRNRFHLLLLGVRQAPPLCEELCQNWFATCEADITCGRTWLWPSGKRSCEGRCRTYGQTFADGVDLCRSVLGHILPVAAPGSRHCLNISISLLPRPRPGRWARETISQRSRRRGTGILDAGGSGSGSGSGSGP | Function: Riboflavin-binding protein which might have a role in retinal flavin transport.
PTM: Not N-glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27236
Sequence Length: 254
Subcellular Location: Secreted
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Q8QZY4 | MAHEGHSQHSGLVWALRPILAWIFLVACGWSHPLQTRSWGHPGLAAKVRTGQLQPAGHPQSSVLPSYPRIQVPGSQTPPVPVPCCTAEIDRPESLLESCGAPSPECEFFLGQLQGALRDRFHPQLFGARPVQPLCPELCQIWFTTCQADFICGPTWLQSSGERGCEPSCRTYGQTFANATDLCHSVLGHVLRVAAPGSSHCLNVSISSPGARRRPRAWISNVVGSGSGSGSGDSPEPMFGFQYVSLP | Function: Riboflavin-binding protein which might have a role in retinal flavin transport.
PTM: Not N-glycosylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26559
Sequence Length: 247
Subcellular Location: Secreted
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Q60335 | MDFIVIDGSYLEGGGQIIRTAVSLSALTQKPVKIINIRKKRKNKGLAPQHVSAVKAVKKLCNAEVFGLNVGSEELTFIPSKLSPKDFTIDIGTAGSISLVIQTLLPLSLGINKKFTVKIKGGTDVKRAPPIDYVKNVTLKILRNFGVLTELKVLKRGFYPEGGGEVIFEVKPSKIKKFDLIEHSKSNLVEGISYVQNLDESIARRMRKKAVDLLNKEKLLPNIKIECSKGISTGAGIVLWNDTLGGSCLGEKGLRAEIVAERAVNELLKERESGMALDKYMGDQIIPFLAFGKGIVGVSEITNHTKTNMWVVKHFLDVDFEIKEYKENNCNGFTIEVV | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (By similarity).
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
Sequence Mass (Da): 37229
Sequence Length: 338
Subcellular Location: Cytoplasm
EC: 6.5.1.4
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O27937 | MIVIDGSEGEGGGAVVRVSTALAAVTSRSVRVYNIRARRSRSGLSHQHLTAVRAVARISNGTLRGDELGSMELEFSPGRVTGGTFNFDVKTAGSTGLVLQAIMVAAAASEGEIDVTVSGGTDVLWAPTCDYLREVTIPVLEMMGYSARIEIIRRGYYPEGGGRVHAIIEPSELRPITLEESEIHAVRGISHSRNLPVHVAERQAESAMKILRGAGLDVDIMVEDASGPVGRGSGITLWAEGNTRLGAVSLGKPGKRAEKVGSEAARELLGFIESGSPLDRYMGDQIIPYMALTGDSRVRTCELTLHAETNIILSEKITGRRFRVEGERGGPATIEVL | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (By similarity).
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
Sequence Mass (Da): 35932
Sequence Length: 337
Subcellular Location: Cytoplasm
EC: 6.5.1.4
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A0B532 | MIEIDGSYGEGGGQIVRTSVALSTLTGIPVRIKNIRRNRPRPGLAAQHVRAIEALAQISRAETRGVHLGSEEIEFIPGRISAGSYDVDIGTAGSVTLLIQCLLPALTAAEGPVTVTVRGGTDVRWSPTVDYLEHVALPAMHLFGVTATFRCERRGYYPRGGGVVVLSTRPSRLRPARLELIEEGICGISHCGSLPEHVARRQADAALELLKEKGYDARIDIQTMSSSSPGSGITLWSGFRGSSALGERGVRAEDVGREAAKALIDELKSKASVDVHLADQLIPYIALAGGEYTTREISSHTRTNIWTAQRILRCRIDIDEGEVFRIHSTGSG | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
Sequence Mass (Da): 35742
Sequence Length: 332
Subcellular Location: Cytoplasm
EC: 6.5.1.4
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Q9D7H3 | MEGQRVEVDGGIMEGGGQILRVSTALSCLLGLPLRVQKIRAGRSTPGLRPQHLSGLEMVRDLCGGHLEGAEIGSTEITFTPEKIRGGVHTADTKTAGSVCLLMQVSMPCVLFAASPSELRLKGGTNAEMAPQIDYTMMVFKPIAEKFGFTFNCDIKTRGYYPKGGGEVIVRVSPVKRLDPINLTDRGSVTKIYGRAFVAGVLPLKVAKDMAAAAVRCIRKEIRDLYVSIQPVQEARDQAFGNGSGIIIVAETSTGCLFAGSSLGKRGVNADKVGIEAAEMLLANLRHGGTVDEYLQDQLIIFMALANGISRIKTGSVTLHTQTAIHFAEQLAKAKFTVKKSEEEEDATKDTYVIECEGIGMANPHL | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (By similarity).
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
Sequence Mass (Da): 39254
Sequence Length: 366
Subcellular Location: Nucleus
EC: 6.5.1.4
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Q2Y720 | MQEIDGSYGEGGGQLLRTSVALAAITGQSVRVYNIRAKRSNPGLAPQHLTAVKAVAALCRARTEGMEVKSQEIIFRPGPLRGGEYDFPIGTAGSVTLVLQAALPVALACGEKVRMNISGGTDVRAAPPLDYFRYVLLPLVYSMGARAKIEVLLRGYYPRGGGKVVVDVEPCLPLRPVLLNASEGLEGITGFVHISNLPKHIIHRMANGALAELSTFPTPAVGLEVFGKDDAIGEGGAVLLTAHKEHSRLGASAVAERGVPAERLGAEAGRCLREEILSGATLDIHAADQVLIYLALASGVSCFLTRELSSHAATTIWLLEQFLPVRFQVTQEAHLIRVRAKPEFNGMSSFLWR | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
Sequence Mass (Da): 37750
Sequence Length: 353
Subcellular Location: Cytoplasm
EC: 6.5.1.4
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B2IWJ8 | MIEIDGSYGEGGGQVLRTSLSLAAITGEPIRIAGIRAGRKKPGLAAQHLTAVRAAGRICNAQLRGDALGSMLLEFIPGSAVQAGIYTFDVSKAQEGGSAGAIALVLQTILLPLALATGNSQVTLKGGTHVNFSPTVTYIEQVYLPILQRMGVEAQVKLGAWGWFPQGGGEIELQVIGGTQLGGINLLERGELQQVRGIAAVTELPSHIPQRMANRAENLLREAHLKVRVQTLREKGVAPGAGIFLTAEYQNSLTGFGGFGRLRLSAETVAEIACQQLLEFHYTGAAVDEHLADQLLLPATLASQESQYQVAEVSRHLITNAAVIEQFGLAQIRVNEADKIVSVKSLTS | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
Sequence Mass (Da): 36859
Sequence Length: 348
Subcellular Location: Cytoplasm
EC: 6.5.1.4
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Q4KEB8 | MKQDVVELDGAIGGGQVLRSALSLSMLTGKTLRIHNIRARRSRPGLLRQHLTAVLAAAQVCGARSTGAELGSQVLSFEPGPIRGGDYRFAIGTAGSCTLVLQTLLPALLRAPQPSRVSISGGTHNPLAPPVDFLQQAWLPQLRRMGGRVELQLLRHGFVPAGGGELEAFIQPSELQPLHLQERGALLGSRAWALSAGLPEHVAERELRRVHDRLQLPREQLTPVLLDEEYGPGNVLLLEFAFEHLTELFCGFGQNSLRAEKVADGAIDQARDWLDSGAAVAEHLADQLLLPMALAGGGSFTTPCMTEHLQSNIRVIEAFLPVRIEARPLSEQVLQVQCHALS | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing.
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
Sequence Mass (Da): 36971
Sequence Length: 342
Subcellular Location: Cytoplasm
EC: 6.5.1.4
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Q9V0Z6 | MITIDGSYGEGGGQILRTSIALSAITGEPVRIINIRANRPNPGLRPQHLHGILALKHLANADVKGAHVGSRELVFIPKRLEAKKVEVNIGTAGSITLVLQALLPAMAFAKNRVEFKITGGTDVPWSPPVDYLANVTLFALEKLGIMAGIKIVRRGHYPKGGGIIEGYVEPWKERRELVATKYSSIAKVEGISHATNLPAHVAERQAKAAKEELSKLEVPVKIKTEVSKSLGPGSGIVVWAETDCLRLGGDALGKRGKPAEVVGKEAAQELLEQLKPGYCVDKFLGDQLIPFLAFSGGEIWVSEVTNHLKTNIWVVENFLGKVFDLDGEVGKPGKVKVVRRVE | Function: Catalyzes the conversion of 3'-phosphate to a 2',3'-cyclic phosphodiester at the end of RNA. The mechanism of action of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA-N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'-phosphorus in the diester linkage to produce the cyclic end product. The biological role of this enzyme is unknown but it is likely to function in some aspects of cellular RNA processing (By similarity).
Catalytic Activity: a 3'-end 3'-phospho-ribonucleotide-RNA + ATP = a 3'-end 2',3'-cyclophospho-ribonucleotide-RNA + AMP + diphosphate
Sequence Mass (Da): 36928
Sequence Length: 342
Subcellular Location: Cytoplasm
EC: 6.5.1.4
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P24931 | MKSLKGSRTEKNILTAFAGESQARNRYNYFGGQAKKDGFVQISDIFAETADQEREHAKRLFKFLEGGDLEIVAAFPAGIIADTHANLIASAAGEHHEYTEMYPSFARIAREEGYEEIARVFASIAVAEEFHEKRFLDFARNIKEGRVFLREQATKWRCRNCGYVHEGTGAPELCPACAHPKAHFELLGINW | Cofactor: Binds 3 Fe(3+) ions per subunit.
Function: May provide oxidative stress protection via catalytic reduction of intracellular hydrogen peroxide.
Sequence Mass (Da): 21544
Sequence Length: 191
Subcellular Location: Cytoplasm
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Q58144 | MINNFFVINMKETLKNLTKAYIGESLARNRYTCYAKIAKQEGYEQIAEIFLLTAENEREHAKWLYYLITELKKKYNIDDKAIKVDGVEVPIVLGNTAENLKASIEGEHFEHTEMYPKFADIAEKEGLKEIADRLRAIGIAEKHHEERFKKLLKEVEEGTVFKKDKPVEWVCRKCGFVHLGKEPPEKCPSCSHPRKYFEVKCEKY | Cofactor: Binds 3 Fe(3+) ions per subunit.
Function: May provide oxidative stress protection via catalytic reduction of intracellular hydrogen peroxide.
Sequence Mass (Da): 23835
Sequence Length: 204
Subcellular Location: Cytoplasm
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Q9AGG3 | MSIKKKTEMNKSIKGSKTEKHLLMAFAGESQARSRYTFFASVAKKEGYEQIAGVFMETAEQEKEHAKRFFSFLEGGMLEITASFPAGIIGSTAENLRAAAAGENEEWTDLYPAFAETAEEEGFKEIAAVFRQIAKVEAEHERRYLALLAHVEDGSVFERTEEIAWQCRNCGYVITSKKAPKLCPACAHPQAYFEPMKTNY | Cofactor: Binds 3 Fe(3+) ions per subunit.
Function: May provide oxidative stress protection via catalytic reduction of intracellular hydrogen peroxide.
Sequence Mass (Da): 22456
Sequence Length: 200
Subcellular Location: Cytoplasm
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Q12234 | MGKNKKKTGKKAKSHPHVEDVDETVNKPEEIINSVNVTVPPKMSTDPEADGIVASPDDEGKDLSEGVDKQKVNDGLTVDTINPLEDKKAGDEMKELREEIERLKLELSHKKDQETPNEDFKNELANVIKERDEFKTQYDTLLSKISSMKSIFNKMKEAQKQLEEVQEQLTEYESQNLKLKKKLEATKTENSELQSTIVTLNTELENLEKEQESTEEVFLEYESRIEALEDEKHDIIEKHSKELNTYRKEKDQLNLQVQELMIILENNKQDISDLRTERDELRQALESHEKEKAVLKNSLNDLELKIEEVDNKREEEARERDQEVKSLRSQLDTEIETHNNDTEALESMKKQLEAMKEDASMKEKYEEESKQHILQIGKLRHEAIILNEHLTKALAMLKKSSDSESVDKELISNLLISFVSIPRADPRKFEVLELLSNFLNWDEDKKQQAGLISNNESKNSSAVSRTESFVSLWTNYLEKESEKD | Function: Involved in the structural organization of the cis-Golgi and in vesicle targeting/fusion stages of ER to Golgi transport.
Sequence Mass (Da): 56069
Sequence Length: 484
Domain: The GRIP domain binds to ARF1, which leads to the Golgi localization of RUD3.
Subcellular Location: Golgi apparatus lumen
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Q96T51 | MADREGGCAAGRGRELEPELEPGPGPGSALEPGEEFEIVDRSQLPGPGDLRSATRPRAAEGWSAPILTLARRATGNLSASCGSALRAAAGLGGGDSGDGTARAASKCQMMEERANLMHMMKLSIKVLLQSALSLGRSLDADHAPLQQFFVVMEHCLKHGLKVKKSFIGQNKSFFGPLELVEKLCPEASDIATSVRNLPELKTAVGRGRAWLYLALMQKKLADYLKVLIDNKHLLSEFYEPEALMMEEEGMVIVGLLVGLNVLDANLCLKGEDLDSQVGVIDFSLYLKDVQDLDGGKEHERITDVLDQKNYVEELNRHLSCTVGDLQTKIDGLEKTNSKLQEELSAATDRICSLQEEQQQLREQNELIRERSEKSVEITKQDTKVELETYKQTRQGLDEMYSDVWKQLKEEKKVRLELEKELELQIGMKTEMEIAMKLLEKDTHEKQDTLVALRQQLEEVKAINLQMFHKAQNAESSLQQKNEAITSFEGKTNQVMSSMKQMEERLQHSERARQGAEERSHKLQQELGGRIGALQLQLSQLHEQCSSLEKELKSEKEQRQALQRELQHEKDTSSLLRMELQQVEGLKKELRELQDEKAELQKICEEQEQALQEMGLHLSQSKLKMEDIKEVNQALKGHAWLKDDEATHCRQCEKEFSISRRKHHCRNCGHIFCNTCSSNELALPSYPKPVRVCDSCHTLLLQRCSSTAS | Function: Binds phospholipid vesicles containing phosphatidylinositol 3-phosphate and participates in early endosomal trafficking.
PTM: Phosphorylation on Tyr-389 and/or Tyr-400 is required for interaction with BMX and endosomal targeting.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 79818
Sequence Length: 708
Domain: The FYVE-type zinc finger domain mediates interactions with phosphatidylinositol 3-phosphate in membranes of early endosomes and penetrates bilayers. The FYVE domain insertion into PtdIns(3)P-enriched membranes is substantially increased in acidic conditions.
Subcellular Location: Cytoplasm
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Q9D394 | MSALTPPTDMPTPTTDKITQAAMETIYLCKFRVSMDGEWLCLRELDDISLTPDPEPTHEDPNYLMANERMNLMNMAKLSIKGLIESALNLGRTLDSDYAPLQQFFVVMEHCLKHGLKAKKTFLGQNKSFWGPLELVEKLVPEAAEITASVKDLPGLKTPVGRGRAWLRLALMQKKLSEYMKALINKKELLSEFYEVNALMMEEEGAIIAGLLVGLNVIDANFCMKGEDLDSQVGVIDFSMYLKDGNSSKGSEGDGQITAILDQKNYVEELNRHLNATVNNLQTKVDLLEKSNTKLTEELAVANNRIITLQEEMERVKEESSYLLESNRKGPKQDRTAEGQALSEARKHLKEETQLRLDVEKELELQISMRQEMELAMKMLEKDVCEKQDALVSLRQQLDDLRALKHELAFKLQSSDLGVKQKSELNSRLEEKTNQMAATIKQLEQSEKDLVKQAKTLNSAANKLIPKHH | Function: Plays a role in the generation of neuronal polarity formation and axon growth . Implicated in the formation of a single axon by developing neurons . May inhibit the formation of additional axons by inhibition of PI3K in minor neuronal processes (By similarity). Plays a role in the formation of F-actin-enriched protrusive structures at the cell periphery (By similarity). Plays a role in cytoskeletal organization by regulating the subcellular localization of FSCN1 and DBN1 at axonal growth cones . Promotes gastric cancer cell migration and invasion in a PAK1-dependent manner (By similarity).
PTM: Phosphorylated by PAK1. Isoform 1 is partially phosphorylated.
Sequence Mass (Da): 53007
Sequence Length: 469
Subcellular Location: Cytoplasm
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Q6ZNE9 | MAEEGAILKVTKDLRAAVSAILQGYGDGQGPVTDTSAELHRLCGCLELLLQFDQKEQKSFLGPRKDYWDFLCTALRRQRGNMEPIHFVRSQDKLKTPLGKGRAFIRFCLARGQLAEALQLCLLNSELTREWYGPRSPLLCPERQEDILDSLYALNGVAFELDLQQPDLDGAWPMFSESRCSSSTQTQGRRPRKNKDAPKKIPAAYGGPENVQIEDSHTSQAICLQDAPSGQQLAGLPRSQQQRHLPFFLEKKGESSRKHRYPQSMWEPEGKELQLDQEERAPWIEIFLGNSTPSTQGQGKGAMGTQKEVIGMEAEVTGVLLVAEGQRTTEGTHKKEAEWSHVQRLLMPSPRGAVEGAVSGSRQGSGGSSILGEPWVLQGHATKEDSTVENPQVQTEVTLVARREEQAEVSLQDEIKSLRLGLRKAEEQAQRQEQLLREQEGELQALREQLSRCQEERAELQAQLEQKQQEAERRDAMYQEELGGQRDLVQAMKRRVLELIQEKDRLWQRLQHLSSMAPECCVACSKIFGRFSRRYPCRLCGGLLCHACSMDYKKRDRCCPPCAQGREAQVT | Function: Positively regulates macroautophagy in primary dendritic cells. Increases autophagic flux, probably by stimulating both autophagosome formation and facilitating tethering with lysosomes. Binds to phosphatidylinositol 3-phosphate (PtdIns3P) through its FYVE-type zinc finger.
Sequence Mass (Da): 64350
Sequence Length: 571
Domain: The RUN domain and the FYVE-type zinc finger are essential for its function in the positive regulation of macroautophagy.
Subcellular Location: Cytoplasmic vesicle
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Q6FFZ9 | MNYQLFKHSDENASYVVFSSGLGGHGSFWQAQLDVFRQYFHVLIYDQEGCHASSELLADGYSFEHLALQVKQLLQQLNIVRFHFIGHALGGFIGIELAHRYASETCQLLSLTLINAWQQLDPHTLRCFTTRIALLQHAGTAAYLHAQALFLYPPLWISEHTALLEQQEAKMQSDFPPHANVLKRLNALMQYQVNTARIDTLKQLPVCLIANQDDMLVPYVQSLNLWKKLPDAQLKLLPYGGHASTVTEARQVNQLMLDFLKTSAPT | Function: Involved in pyrimidine catabolism. May facilitate the hydrolysis of carbamate, a reaction that can also occur spontaneously.
Catalytic Activity: carbamate + 2 H(+) = CO2 + NH4(+)
Sequence Mass (Da): 30161
Sequence Length: 266
EC: 3.5.1.-
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Q7CWX3 | MHFEVHGRTDAEAPTILLSSGLGGSSAYWLPQIEALSDHFRIVTYDHRGTGRTGGEVPTEGGISAMADDVLEIVSALNLEKFHFMGHALGGLIGLDIALRQPRLIDRLVLINAWSKADPHSGRCFDVRIELLEKSGVDAFVKAQPLFLYPAAWMSEHQERLARDDAHGVAHFQGKTNVLRRIAALRAFDIDARLGEIGNPVLVVATKDDLLVPYTRSLRLAEGLPQSELCLLDFGAHAVNITEPDLFNTRLLQFLLPADQT | Function: Involved in pyrimidine catabolism. May facilitate the hydrolysis of carbamate, a reaction that can also occur spontaneously.
Catalytic Activity: carbamate + 2 H(+) = CO2 + NH4(+)
Sequence Mass (Da): 28691
Sequence Length: 261
EC: 3.5.1.-
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A8IAD8 | MPYAHGGDADLYYEIHGAGTPILLSAGMGGGAGFWRPQIEALAARHQVILYDHAGTGRSGRDIGPRSITEMARDMARVLDAAGVEDAHVAGHAIGGIIGMELALAAPERVRSLTIVNGWARADGFLRRCFEVRKRILLASGPEAYVRAQPLFLYPPRWIAENIAVLEEEEAQMVAHFPGTQTMLNRIETFLAFDGRERLADIRVPTLLAAAKDDALVPSYLSTLLAEGIPDARIAEVDWGAHAFSAVTPDVFNEMLLGFCGEIDQ | Function: Involved in pyrimidine catabolism. May facilitate the hydrolysis of carbamate, a reaction that can also occur spontaneously.
Catalytic Activity: carbamate + 2 H(+) = CO2 + NH4(+)
Sequence Mass (Da): 28703
Sequence Length: 265
EC: 3.5.1.-
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Q9A4N3 | MRRMTIGTVDGLHYELHGGPIAGREVVLLSSGLGGSGAFWAPQMQALTQRWPVVTYDHRGTGRSVRELPPRYTLAHMADDMVKVMDALGLAKAHVVGHAAGGNAGLQLALDHPDRLAKLVVVNGWSRPDPHIRRCFDTRLHLLNDTGPEAYVHAQPIFLYPADWISRNHTRLMAEEAHHVAAFPPREVMLARINALLAFDIDARLEDITHRVLISASADDMLVPMSCSQRLAGRLPNADFQQVAWGGHGFTVTDPETFNEALVSFLEGA | Function: Involved in pyrimidine catabolism. May facilitate the hydrolysis of carbamate, a reaction that can also occur spontaneously.
Catalytic Activity: carbamate + 2 H(+) = CO2 + NH4(+)
Sequence Mass (Da): 29553
Sequence Length: 269
EC: 3.5.1.-
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C8U5H1 | MKLSLSPPPYADAPVVVLISGLGGSGSYWLQQLAVLEQEYQVVCYDQRGTGNNPDTLAEDYSIAQMAAELHQALVAAGIEHYAVVGHALGALVGMQLALDYPASVTVLISVNGWLRINAHTRRCFQVRERLLYSGGAQAWVEAQPLFLYPADWMAARAPRLEAEDALALAHFQGKNNLLRRLNALKRADFSHHADRIRCPVQIICASDDLLVPTACSSELHAALPDSQKMVMPYGGHACNVTDPETFNALLLNGLASLLHHREAAL | Function: Involved in pyrimidine catabolism. May facilitate the hydrolysis of carbamate, a reaction that can also occur spontaneously.
Catalytic Activity: carbamate + 2 H(+) = CO2 + NH4(+)
Sequence Mass (Da): 28929
Sequence Length: 266
EC: 3.5.1.-
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C1F8Z2 | MIAHLRGTLLSKQPGQAIVECAGVGYDVAISVPTFTALPAEGAEVRLHIHTQVSEDAIALFGFLDREEKRLFERLITVSGVGPKLAIKMLSGLSPERTVAALRAQDHASLTRIPGVGKKLAERLVVELKDKLDDLIAAAPAAGPVAAGPAAEDVLSALLNLGYQRPAALKAIETAVEKDAAAGEDFDLLFRAALKLIR | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 20903
Sequence Length: 198
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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A5G2L3 | MIGRLCGTAEQIEDGRCLIDVSGVGYVVFCSARSLAALPAPPARATLLVETQVREDAITLFGFIDAAERDWFRLLTTIQGVGAKVALNLLSALPPDQLASAIAASDRGAITRAPGVGPKLAARLISELRERIAAMPTGSAFIPTGTAPPVAPPQGKLADALSALVNLGYRRAEAEAALSAVQAEAGEDAALDELIRGGLRRLAR | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 21164
Sequence Length: 204
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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B7J3G2 | MITSLTGTILQRRPPWLWLDVQGVGYELEMPLSGFYQMPAEGAALTVHTHLTIREDAHLLYGFMTVAERDMFRLLIRVNGIGGKVALACLSGLPAERLSQAVAEGNTAQLTAIPGIGPKTAERLVVELRDKMGGIAPGPMGRGGAGDPRQEAIAALLTLGYKPAQASQAIAGLADGLGLEDLIRQSLQNLSRH | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 20547
Sequence Length: 193
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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A0KPA3 | MIGRLRGVVIEKQPPEVLLEVGGVGYEVQMPMSCFYDLPEIGKEATIHTHFVVREDAQLLYGFNHKQERALFRELIKTNGVGPKLALAILSGMTATQFVLSVEREEISSLVKLPGVGKKTAERLVVEMKDRLKGWVSHDLFSPAEITLPARESALRAPDSSEEAASALVALGYKPQQASQIVSKVAADGMSVEDIIREALRSLV | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 22353
Sequence Length: 204
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
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Q8U9K5 | MIGKLKGSIEEIGADYVLVDVHGVCYVAYCSARTLSKIGSVGEAVVLFIETYVREDQLKLFGFVSALEREWFNLLQSVQGVGSKVALAVLSTLSPSELANAIALQDKTMISRAPGIGPKVAVRLVTELRNKAPAFAGDASASIGLKQELGEGVASAPVADAVSALTNLGYSRDQAANAVAAALKNGGEGGDSAKLIRLGLKELSR | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 21320
Sequence Length: 205
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
|
Q5E6A0 | MIGRLRGNLLEKQPPELLIEVSGIGYEVQMPMSCFYELPEVGSEAIIYTHYVVREDAQLLYGFNTKNERALFREVIKANGVGPKLGLAILSGMTAAQFVQSVEREDISTLVKLPGVGKKTAERLVVEMKDRLKGWGAGDLFTPATDAAPMDDGSEFITSPQSAVDEAVSALIALGYKPQQASKTVSQIAKPDMTSEVLIRESLKSMI | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 22565
Sequence Length: 207
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
|
P44632 | MIGRLQGILLEKQPPEILLNVQGVGYELLLPMTSFYDLPEIGQETTLFTHLVVREDAHLLFGFAQKTDRTLFRELIKTNGVGPKLALAILSAMSVEQFAYAIEREELSKLTKIPGVGKKTAERLLVELKGKFKGVKQSDFFVESTHIPLSPSIESHSESSSDEAISALIALGYKPVEAEKMVKRVAKPELTSEQVIREALKVAL | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 22603
Sequence Length: 204
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
|
A1WZ64 | MIARLRGTLLEKRPPTLVVEANGLGYEVEAPLSTIEALPETGREVILHTHLSVREDGQTLFGFRTRAERDLFRRLIRVSGVGPKLGLALLSGVDGEELVRCVRDDDPKRLTQVPGIGRKTAERLIVELRDRLDGVGGGSTAAPAAGADHPTGENDPVSEAIEGLVALGYKPPEAARMARNAAEPELGCEAIIRRALQRAVPRGG | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 21876
Sequence Length: 204
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
|
B8CXG3 | MIGYLKGNVIWKAENKVILETGGVGYRVLVPSTVRLKPVGEKLELFVYTYVREDSLDLYGFKTMEERELFETLLSVSGIGPRAAINILSSLSYKKFIEAILTEKVSILKQVSGIGPKTAKRLILELKGKLKDMSGDFEEPLPDNRNTELSDALASLGYSELEIEEALSNADIKNNGSLEENIKKALGYLGSKGS | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 21392
Sequence Length: 194
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
|
C4K7I5 | MISRMKGIILEKQPPWILLDIQGMGYDIQLPMTCFYQLPELGQEAIIFTHFVVREDAQLLYGFHHPKERAMFSELIKVNGVGPKLGLAILSGMSSEEFICALEKEDISNLIKLPGVGKKTAERLLVEMKDRIKNLNKNLFKSTADHMLSSVSTDLSAKSAEAEAISALISLGYKPQEAAQLIKNIAQPDLDSQALIKHALRSTL | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 22663
Sequence Length: 204
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
|
O25549 | MIVGLIGVVEKISALEVHIEVQGVVYGVQVSMRTAALLEAGQKARLKILQVIKEDAHLLYGFLEEGEKILFERLLKINGVGGRIALAILSSFSPNEFESIIATKEVKRLQQVPGIGKKLADKIMVDLIGFFIQDENRPARNEVFLALESLGFKSAEINQVLKTLKPNLSIEAAIKEALQQLRS | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 20176
Sequence Length: 183
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
|
Q5YTE7 | MIASVRGEVLEIALDHVVVEAAGVGYRLNATPSTLATLTRGAEARLYTAMIVREDSMTLYGFADTEARDLFGLLQTVSGVGPRLAMAVLAVLEPEALRKALAESNVAALTRVPGIGKRGAERMVVELRDKVNLVPVQAGPPGSTPAVAATPVREQVVEALTGLGFPLKQAEQALDTVLAEQPAADTSTALRAALSLLGKNR | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 21021
Sequence Length: 201
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
|
Q8EPQ5 | MIAYIKGTLNSLGDESLIVDVGGIGYEIVCPNPFVFQDLLNQQIHIQTYHHVREDAQILFGFQNRDEKYLFTKLISVSGIGPKGALAILAGVDISGFIAAVENEDDKFLTSFPGVGKKTARQIILDLKGKLTSVFSITDEQQKSSVSNVNNNEVYSEAMEALKALGYTDKEVKQVLPHLKKDNDALSVDEAIRKALALLAK | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 22041
Sequence Length: 201
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
|
B1ZN17 | MITSIQGTLVSATPLQAIVEVAGFGYEVHIPVTTAERLPAAGAAVKLHTLVIYREDSQTLYGFASPAERDFFRLMIEHVTGVGPKMALSIMSRLALPSLESAIRMGDVASLAKCPGIGKKTAERLVVELRTKVGATGAAPGLATQPAAAASPGASAHRDAVAALVALGYRSADADEAVRRASLALGEAATTESLIKKALS | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 20620
Sequence Length: 200
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
|
A1AZW3 | MIGRIAGVILHRAQDHVLIDVRGVGYIVHVSERTAANLPPAGQATALYTELLVREDLLQLFGFPTLLEKEWHRLLTSVQGVGAKVALAILGTLGPDGLSRALALGDWSALRKAPGVGPKLAQRVVMELKDKAPAVMALGGALTVDPGPLPEVELVEAAVPAPVPAKAAPSSAQATADALSALGNLGYAPSEAASAVAEAAAREPAAPTAALIRAALRLLAPKE | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 22846
Sequence Length: 223
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
|
Q7U7F0 | MIGWLKGDVQHRDQKGSRNLVLIACGGVGYDVQLIERDWQAVSTDQRHEFWIHQVVSADNLQLFGFLQLAERDLFRELIQVSGVGPQAGLALLNACAYKELVTALVHSDLKTLCRAKGVGKRTAERLALELRTRLTDSVASTGPERNQLDPVAPDLIATLETLGFETHEIRDALQRLNGMGGPQDGDDDDAWLRACIKLMSSTDP | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 22645
Sequence Length: 205
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
|
Q6MFA5 | MFAYIKGVLAFFNPSQAIVDVHGVGYLLFIPCRLLGQLPQIGEPVQFYTTYVVREFSHTLYGFLSYQERDIFEILMNVTGIGPKMALSLIGHLSMSELQIAVMRQDLSTLCRVPGVGKKTAERLIVELKDKLAAIGHLDTSDHIEPLTQDPKSKSVQDAMLALINLGYNQTTAQKAIKQGMKELPEEIDLAQLITVALKHV | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 22342
Sequence Length: 201
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
|
Q83GK0 | MIASLSGLLEAVRPGSVVVNMHGIGFLVRVPQSFNPEVDAEVKLYTSLQVREDSVSLYGFASVLECTVFEQLITISGVGPRVALAILSVLTPAEVAAAVLEGDDKPLQRVSGVGKKLAGTIVLQLAGKLTSVPLENRKQEQAVDRSAEIVQALIGLGWQRQESAAAVESVLEKDQSLTMPEILRNALRYLAKQE | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 20791
Sequence Length: 194
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
|
B5ZBT6 | MNYLVFKVIYANANVVIGEHNFIGYQIRVPKDYELEVNKFCKLYLYEYASIMPNKNLIIKDLYGFRTYNERLLFIDLISINSIGPKTAINILKYDINLIIDAIATKDVDFLATIKGVNQRSANLICDQLNYKYINKVSEKNPWAKELSIGLENLGYDKKDIEYAITKVKVDTQQNIDISEIIGCAIKEISLRHEN | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 22512
Sequence Length: 195
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
|
Q87QU8 | MIGRLRGILLEKQPPEVLIEVNGIGYEVQMPMSCFYELPNIGEEAIIYTHFVVREDAQLLYGFNTVKERALFREVIKANGVGPKLGLGILSGMTASQFVSCVEREDVSTLVKLPGVGKKTAERLVVEMKDRLKGWGAGDLFTPFTDAAPTDSAAASSNSAEEEAVSALLALGYKPTQASKVVSQIAKPDMSSEQLIREALKSMV | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA.
Sequence Mass (Da): 22123
Sequence Length: 204
Domain: Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB.
Subcellular Location: Cytoplasm
|
Q9PMT7 | MDRIVEIEKYSFDETYETSLRPSNFDGYIGQESIKKNLNVFIAAAKKRNECLDHILFSGPAGLGKTTLANIISYEMSANIKTTAAPMIEKSGDLAAILTNLSEGDILFIDEIHRLSPAIEEVLYPAMEDYRLDIIIGSGPAAQTIKIDLPKFTLIGATTRAGMLSNPLRDRFGMQFRLEFYKDSELALILQKAALKLNKTCEEKAALEIAKRSRSTPRIALRLLKRVRDFADVNDEEIITEKRANEALNSLGVNELGFDAMDLRYLELLTAAKQKPIGLASIAAALSEDENTIEDVIEPYLLANGYIERTAKGRIASAKSYSALKLNYEKTLFEE | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 37312
Sequence Length: 335
Domain: Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S) domains and the C-terminal head (RuvB-H) domain. The head domain binds DNA, while the ATPase domains jointly bind ATP, ADP or are empty depending on the state of the subunit in the translocation cycle. During a single DNA translocation step the structure of each domain remains the same, but their relative positions change.
Subcellular Location: Cytoplasm
EC: 3.6.4.12
|
Q9A3G8 | MTRVISGEPQHGDLAPADRALRPQTLAEFVGQEQAKGNLRVFIEAAKGRGEALDHVLLFGPPGLGKTTLAQIVARELGVNFRATSGPVLNKPGDLAAILTNLEANDVLFIDEIHRLSSNVEEILYPAMEDHVLDLVIGEGPSARSIRIDLAPFTLVAATTRAGMLATPLRDRFGIPIRLEFYTPAELRHVLQHAARKMGAPLTDDGADEIAKRARGTPRVAGRLLRRVRDFATADGADRIDRKAAAMALARLEVDESGLDSLDRRYLRAMIENYGGGPVGVETIAYAIAEARDAVEDVIEPYLMQQGFIQRTPRGRMACGKAYLHLGLTPPAAPPGQAQGALFDEG | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 37360
Sequence Length: 346
Domain: Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S) domains and the C-terminal head (RuvB-H) domain. The head domain binds DNA, while the ATPase domains jointly bind ATP, ADP or are empty depending on the state of the subunit in the translocation cycle. During a single DNA translocation step the structure of each domain remains the same, but their relative positions change.
Subcellular Location: Cytoplasm
EC: 3.6.4.12
|
Q600N3 | MPENLEIRPSSFENFIGQKKLVETLQILISSSQKRKQSLDHILFYGPPGTGKTTLANIVANVLEAKIKYVQGPLLEKKSDVLAVLANISPDTIIFIDEIHGINKNIEELLYSAMEEFVIDLQIGVDGERKIMRMKLPQFTLIGASTKLAQISTPLQNRFGYVAKIVDYTLEDMIQIIRNSSAVLKLKMNTEIIKYIASFSNNTPRIANNLLKRIRDFALVLNAKRIDKDIVNKTFDSIGIYNQGLSQINIEYLNLLVKIFKGKSVALDVIANVLKEHRQTIINIIEPPLIEKELIEKTSRGRRITKKGRDYLLELKTN | Function: The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. RuvB forms 2 homohexamers on either side of HJ DNA bound by 1 or 2 RuvA tetramers; 4 subunits per hexamer contact DNA at a time. Coordinated motions by a converter formed by DNA-disengaged RuvB subunits stimulates ATP hydrolysis and nucleotide exchange. Immobilization of the converter enables RuvB to convert the ATP-contained energy into a lever motion, pulling 2 nucleotides of DNA out of the RuvA tetramer per ATP hydrolyzed, thus driving DNA branch migration. The RuvB motors rotate together with the DNA substrate, which together with the progressing nucleotide cycle form the mechanistic basis for DNA recombination by continuous HJ branch migration. Branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves cruciform DNA.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 36062
Sequence Length: 318
Domain: Has 3 domains, the large (RuvB-L) and small ATPase (RuvB-S) domains and the C-terminal head (RuvB-H) domain. The head domain binds DNA, while the ATPase domains jointly bind ATP, ADP or are empty depending on the state of the subunit in the translocation cycle. During a single DNA translocation step the structure of each domain remains the same, but their relative positions change.
Subcellular Location: Cytoplasm
EC: 3.6.4.12
|
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